Structural analysis of a ligand-triggered intermolecular disulfide switch in a major latex protein from opium poppy.

ABSTRACT: Several proteins from plant pathogenesis-related family 10 (PR10) are highly abundant in the latex of opium poppy and have recently been shown to play diverse and important roles in the biosynthesis of benzylisoquinoline alkaloids (BIAs). The recent determination of the first crystal structures of PR10-10 showed how large conformational changes in a surface loop and adjacent β-strand are coupled to the binding of BIA compounds to the central hydrophobic binding pocket. A more detailed analysis of these conformational changes is now reported to further clarify how ligand binding is coupled to the formation and cleavage of an intermolecular disulfide bond that is only sterically allowed when the BIA binding pocket is empty. To decouple ligand binding from disulfide-bond formation, each of th

SUBMITTER: Carr SC 

PROVIDER: S-EPMC11394122 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature